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Volumn 120, Issue 3, 2004, Pages 370-385

Modelling NADH turnover in plant mitochondria

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; OXIDATION; PH EFFECTS;

EID: 1542543858     PISSN: 00319317     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.0031-9317.2003.00252.x     Document Type: Article
Times cited : (32)

References (40)
  • 1
    • 0032425311 scopus 로고    scopus 로고
    • The internal rotenone-insensitive NADPH dehydrogenase contributes to malate oxidation by potato tuber and pea leaf mitochondria
    • Agius SC, Bykova NV, Igamberdiev AU, Møller IM (1998) The internal rotenone-insensitive NADPH dehydrogenase contributes to malate oxidation by potato tuber and pea leaf mitochondria. Physiol Plant 104: 329-336
    • (1998) Physiol Plant , vol.104 , pp. 329-336
    • Agius, S.C.1    Bykova, N.V.2    Igamberdiev, A.U.3    Møller, I.M.4
  • 3
    • 0000974248 scopus 로고
    • NAD-malic enzyme from plants
    • Artus NN, Edwards GE (1985) NAD-malic enzyme from plants. FEBS Lett 182: 225-233
    • (1985) FEBS Lett , vol.182 , pp. 225-233
    • Artus, N.N.1    Edwards, G.E.2
  • 5
    • 0034742737 scopus 로고    scopus 로고
    • +-linked substrates by pea leaf mitochondria
    • +-linked substrates by pea leaf mitochondria. Physiol Plant 111: 448-456
    • (2001) Physiol Plant , vol.111 , pp. 448-456
    • Bykova, N.V.1    Møller, I.M.2
  • 6
    • 0037431026 scopus 로고    scopus 로고
    • Identification of 14 new phosphoproteins involved in important plant mitochondrial processes
    • Bykova NV, Egsgaard H, Møller IM (2003) Identification of 14 new phosphoproteins involved in important plant mitochondrial processes. FEBS Lett 540: 141-146
    • (2003) FEBS Lett , vol.540 , pp. 141-146
    • Bykova, N.V.1    Egsgaard, H.2    Møller, I.M.3
  • 8
    • 78651031094 scopus 로고
    • The respiratory chain and oxidative phosphorylation
    • Chance B, Williams GR (1956) The respiratory chain and oxidative phosphorylation. Adv Enzymol Rel S Bi 17: 65-134
    • (1956) Adv Enzymol Rel S Bi , vol.17 , pp. 65-134
    • Chance, B.1    Williams, G.R.2
  • 9
    • 0021763602 scopus 로고
    • Activation of NAD-linked malic enzyme in intact plant mitochondria by exogenous coenzyme A
    • Day DA, Neuburger M, Douce R (1984) Activation of NAD-linked malic enzyme in intact plant mitochondria by exogenous coenzyme A. Arch Biochem Biophys 231: 233-242
    • (1984) Arch Biochem Biophys , vol.231 , pp. 233-242
    • Day, D.A.1    Neuburger, M.2    Douce, R.3
  • 11
  • 12
    • 0035253217 scopus 로고    scopus 로고
    • Macromolecular crowding: An important but neglected aspect of the intracellular environment
    • Ellis RJ (2001) Macromolecular crowding: an important but neglected aspect of the intracellular environment. Curr Opinion Struct Biol 11: 114-119
    • (2001) Curr Opinion Struct Biol , vol.11 , pp. 114-119
    • Ellis, R.J.1
  • 13
    • 0013936320 scopus 로고
    • Ultrastructural bases for metabolically linked mechanical activity in mitochondria. I. Reversible ultrastructural changes with change in metabolic steady state in isolated liver mitochondria
    • Hackenbrock CR (1966) Ultrastructural bases for metabolically linked mechanical activity in mitochondria. I. Reversible ultrastructural changes with change in metabolic steady state in isolated liver mitochondria. J Cell Biol 30: 269-297
    • (1966) J Cell Biol , vol.30 , pp. 269-297
    • Hackenbrock, C.R.1
  • 14
    • 0014409086 scopus 로고
    • Kinetic studies on the mechanism of the malate dehydrogenase reaction
    • Heyde E, Ainsworth S (1968) Kinetic studies on the mechanism of the malate dehydrogenase reaction. J Biol Chem 243: 2413-2423
    • (1968) J Biol Chem , vol.243 , pp. 2413-2423
    • Heyde, E.1    Ainsworth, S.2
  • 15
    • 0035975695 scopus 로고    scopus 로고
    • A model of oxidative phosphorylation in mammalian skeletal muscle
    • Korzeniewski B, Zoladz JA (2001) A model of oxidative phosphorylation in mammalian skeletal muscle. Biophys Chem 92: 17-34
    • (2001) Biophys Chem , vol.92 , pp. 17-34
    • Korzeniewski, B.1    Zoladz, J.A.2
  • 16
    • 0025964378 scopus 로고
    • Respiration of pea leaf mitochondria and redox transfer between the mitochondrial and extramitochondrial compartments
    • Krömer S, Heldt HW (1991) Respiration of pea leaf mitochondria and redox transfer between the mitochondrial and extramitochondrial compartments. Biochim Biophys Acta 1057: 42-50
    • (1991) Biochim Biophys Acta , vol.1057 , pp. 42-50
    • Krömer, S.1    Heldt, H.W.2
  • 17
    • 0015055552 scopus 로고
    • Isolation and properties of a 'malic' enzyme from cauliflower bud mitochondria
    • Macrae AR (1971) Isolation and properties of a 'malic' enzyme from cauliflower bud mitochondria. Biochem J 122: 495-501
    • (1971) Biochem J , vol.122 , pp. 495-501
    • Macrae, A.R.1
  • 18
    • 0035781005 scopus 로고    scopus 로고
    • Plant mitochondria and oxidative stress: Electron transport, NADPH turnover, and metabolism of reactive oxygen species
    • Møller IM (2001) Plant mitochondria and oxidative stress: Electron transport, NADPH turnover, and metabolism of reactive oxygen species. Annu Rev Plant Physiol Plant Mol Biol 52: 561-591
    • (2001) Annu Rev Plant Physiol Plant Mol Biol , vol.52 , pp. 561-591
    • Møller, I.M.1
  • 19
    • 0001115403 scopus 로고
    • Membrane-bound NAD (P) H dehydrogenases in higher plant cells
    • Møller IM, Lin W (1986) Membrane-bound NAD (P) H dehydrogenases in higher plant cells. Annu Rev Plant Physiol 37: 309-334
    • (1986) Annu Rev Plant Physiol , vol.37 , pp. 309-334
    • Møller, I.M.1    Lin, W.2
  • 20
    • 84986974453 scopus 로고
    • Direct evidence for the presence of a rotenone-resistant NADH dehydrogenase on the inner surface of the inner membrane of plant mitochondria
    • Møller IM, Palmer JM (1982) Direct evidence for the presence of a rotenone-resistant NADH dehydrogenase on the inner surface of the inner membrane of plant mitochondria. Physiol Plant 54: 267-274
    • (1982) Physiol Plant , vol.54 , pp. 267-274
    • Møller, I.M.1    Palmer, J.M.2
  • 21
    • 0000063667 scopus 로고
    • Regulation of the tricarboxylic acid cycle and organic acid metabolism
    • Palmer JM (ed) Cambridge University Press, Cambridge
    • Møller IM, Pakner JM (1984) Regulation of the tricarboxylic acid cycle and organic acid metabolism. In: Palmer JM (ed) The Physiology and Biochemistry of Plant Respiration. Cambridge University Press, Cambridge, pp. 105-122
    • (1984) The Physiology and Biochemistry of Plant Respiration , pp. 105-122
    • Møller, I.M.1    Pakner, J.M.2
  • 22
    • 0031952559 scopus 로고    scopus 로고
    • The role of NADP in the mitochondrial matrix
    • Møller IM, Rasmusson AG (1998) The role of NADP in the mitochondrial matrix. Trends Plant Sci 3: 21-27
    • (1998) Trends Plant Sci , vol.3 , pp. 21-27
    • Møller, I.M.1    Rasmusson, A.G.2
  • 23
    • 0001405510 scopus 로고
    • The regulation of malate oxidation in plant mitochondria by the redox state of endogenous pyridine nucleotides
    • Neuburger M, Day DA, Douce R (1984) The regulation of malate oxidation in plant mitochondria by the redox state of endogenous pyridine nucleotides. Physiol Vég 22: 571-580
    • (1984) Physiol Vég , vol.22 , pp. 571-580
    • Neuburger, M.1    Day, D.A.2    Douce, R.3
  • 24
    • 1542626728 scopus 로고
    • Regulation of NAD(P)H dehydrogenases in plant mitochondria
    • Palmer JM, Møller IM (1982) Regulation of NAD(P)H dehydrogenases in plant mitochondria. Trends Biochem Sci 7: 258-261
    • (1982) Trends Biochem Sci , vol.7 , pp. 258-261
    • Palmer, J.M.1    Møller, I.M.2
  • 26
  • 27
    • 0030048345 scopus 로고    scopus 로고
    • Oxygen concentration and the oxidation-reduction state of yeast: Determination of free/bound NADH and flavins by time-resolved spectroscopy
    • Paul RJ, Schneckenburger H (1996) Oxygen concentration and the oxidation-reduction state of yeast: Determination of free/bound NADH and flavins by time-resolved spectroscopy. Naturwissenschaften 83: 32-35
    • (1996) Naturwissenschaften , vol.83 , pp. 32-35
    • Paul, R.J.1    Schneckenburger, H.2
  • 28
    • 0034973677 scopus 로고    scopus 로고
    • Dissecting the superoxide dismutase-ascorbate-glutathione-pathway in chloroplasts by metabolic modeling. Computer simulations as a step towards flux analysis
    • Polle A (2001) Dissecting the superoxide dismutase-ascorbate-glutathione- pathway in chloroplasts by metabolic modeling. Computer simulations as a step towards flux analysis. Plant Physiol 126: 445-462
    • (2001) Plant Physiol , vol.126 , pp. 445-462
    • Polle, A.1
  • 30
    • 84989674612 scopus 로고
    • NAD (P) H dehydrogenases on the inner surface of the inner mitochondrial membrane studied using inside-out submitochondrial particles
    • Rasmusson AG, Møller IM (1991) NAD (P) H dehydrogenases on the inner surface of the inner mitochondrial membrane studied using inside-out submitochondrial particles. Physiol Plant 83: 357-365
    • (1991) Physiol Plant , vol.83 , pp. 357-365
    • Rasmusson, A.G.1    Møller, I.M.2
  • 31
    • 0001190793 scopus 로고
    • Malate oxidation in plant mitochondria via malic enzyme and the cyanide-insensitive electron transport pathway
    • Rustin P, Moreau F, Lance C (1980) Malate oxidation in plant mitochondria via malic enzyme and the cyanide-insensitive electron transport pathway. Plant Physiol 66: 457-462
    • (1980) Plant Physiol , vol.66 , pp. 457-462
    • Rustin, P.1    Moreau, F.2    Lance, C.3
  • 32
    • 30244573126 scopus 로고
    • Emission properties of NADH. Studies of fluorescence lifetimes and quantum efficiencies of NADH, AcPyADH, and simplified synthetic models
    • Scott TG, Spencer RD, Leonard NJ, Weber G (1970) Emission properties of NADH. Studies of fluorescence lifetimes and quantum efficiencies of NADH, AcPyADH, and simplified synthetic models. J Am Chem Soc 92: 687-695
    • (1970) J Am Chem Soc , vol.92 , pp. 687-695
    • Scott, T.G.1    Spencer, R.D.2    Leonard, N.J.3    Weber, G.4
  • 33
    • 0001967031 scopus 로고    scopus 로고
    • Respiration and Photorespiration
    • Buchanan BB, Gruissem W, Jones RL (ed) American Society of Plant Physiologists, Rockville, MD
    • Siedow JN, Day DA (2000) Respiration and Photorespiration. In: Buchanan BB, Gruissem W, Jones RL (ed) Biochemistry & Molecular Biology of Plants. American Society of Plant Physiologists, Rockville, MD, pp. 676-728.
    • (2000) Biochemistry & Molecular Biology of Plants , pp. 676-728
    • Siedow, J.N.1    Day, D.A.2
  • 34
    • 0018854310 scopus 로고
    • The infrastructure of the mitochondrial matrix
    • Srere PA (1980) The infrastructure of the mitochondrial matrix. Trends Biochem Sci 5: 120-121
    • (1980) Trends Biochem Sci , vol.5 , pp. 120-121
    • Srere, P.A.1
  • 35
    • 0001885173 scopus 로고
    • Protein crystals as a model for mitochondrial matrix proteins
    • Srere PA (1981) Protein crystals as a model for mitochondrial matrix proteins. Trends Biochem Sci 6: 4-7
    • (1981) Trends Biochem Sci , vol.6 , pp. 4-7
    • Srere, P.A.1
  • 37
    • 0028859022 scopus 로고
    • Alternative oxidase activity in tobacco leaf mitochondria - Dependence on tricarboxylic acid cycle-mediated redox regulation and pyruvate activation
    • Vanlerberghe GC, Day DA, Wiskich JT, Vanlerberghe AE, McIntosh L (1995) Alternative oxidase activity in tobacco leaf mitochondria - dependence on tricarboxylic acid cycle-mediated redox regulation and pyruvate activation. Plant Physiol 109: 353-361
    • (1995) Plant Physiol , vol.109 , pp. 353-361
    • Vanlerberghe, G.C.1    Day, D.A.2    Wiskich, J.T.3    Vanlerberghe, A.E.4    McIntosh, L.5
  • 38
    • 0033018484 scopus 로고    scopus 로고
    • Characterization of two members of a novel malic enzyme class
    • Voegele RT, Mitsch MJ, Finan TM (1999) Characterization of two members of a novel malic enzyme class. Biochim Biophys Acta 1432: 275-285
    • (1999) Biochim Biophys Acta , vol.1432 , pp. 275-285
    • Voegele, R.T.1    Mitsch, M.J.2    Finan, T.M.3
  • 39
    • 0029608708 scopus 로고
    • Some characteristics of the fluorescence lifetime of reduced pyridine nucleotides in isolated mitochondria, isolated hepatocytes, and perfused rat liver in situ
    • Wakita M, Nishimura G, Tamura M (1995) Some characteristics of the fluorescence lifetime of reduced pyridine nucleotides in isolated mitochondria, isolated hepatocytes, and perfused rat liver in situ. J Biochem 118: 1151-1160
    • (1995) J Biochem , vol.118 , pp. 1151-1160
    • Wakita, M.1    Nishimura, G.2    Tamura, M.3
  • 40
    • 0542361843 scopus 로고
    • Physical and kinetic properties and regulation of the NAD malic enzyme purified from leaves of Crassula argentea
    • Wedding RT, Black MK (1983) Physical and kinetic properties and regulation of the NAD malic enzyme purified from leaves of Crassula argentea. Plant Physiol 72: 1021-1028
    • (1983) Plant Physiol , vol.72 , pp. 1021-1028
    • Wedding, R.T.1    Black, M.K.2


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